Molecular interaction between human SUMO-I and histone like DNA binding protein of Helicobacter pylori (Hup) investigated by NMR and other biophysical tools
| Autor: | Sarita Tripathi, Venus Singh Mithu, Krishna Mohan Poluri, Dinesh Kumar, Ashish Arora, Nancy Jaiswal, Anupreet Kaur, Gagandeep Kaur Gahlay, Nipanshu Agarwal |
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| Rok vydání: | 2019 |
| Předmět: |
Sequence analysis
Amino Acid Motifs SUMO-1 Protein Lysine RNA-binding protein 02 engineering and technology Biochemistry DNA-binding protein 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Structural Biology Humans Nuclear Magnetic Resonance Biomolecular Molecular Biology 030304 developmental biology 0303 health sciences Helicobacter pylori biology General Medicine 021001 nanoscience & nanotechnology biology.organism_classification In vitro DNA-Binding Proteins Histone chemistry biology.protein 0210 nano-technology DNA Bacteria Protein Binding |
| Zdroj: | International Journal of Biological Macromolecules. 123:446-456 |
| ISSN: | 0141-8130 |
| Popis: | The proteins secreted by bacteria contribute to immune mediated gastric inflammation and epithelial damage; thus aid bacterial invasion in host tissue, and may also interact with host proteins, conspirating a mechanism against host-immune system. The Histone-like DNA binding protein is one of the most abundant nucleoid-associated proteins in Helicobacter pylori (H. pylori). The protein -referred here as Hup- is also secreted in vitro by H. pylori, thus it may have its role in disease pathogenesis. This is possible only if Hup interact with some human proteins including Small-Ubiquitin-like-Modifier (SUMO) proteins. Studies have established that SUMO-proteins participate in various innate-immune pathways and thus promote an efficient immune response to combat pathogenic infections. Sequence analysis revealed the presence of two SUMO interacting motifs (SIMs) and several positively charged lysine residues on the protein surface of Hup. Additionally, SUMO-proteins epitomize negatively charged surface which confers them the ability to bind to DNA/RNA binding proteins. Based on the presence of SIMs as well as charge complementarity between the proteins, it is legitimate to consider that Hup protein would bind to SUMO-proteins. The present study has been undertaken to establish this interaction for the first time using NMR in combination with ITC and other biophysical techniques. |
| Databáze: | OpenAIRE |
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